ID A0A0K9GF49_9BACI Unreviewed; 639 AA.
AC A0A0K9GF49;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=AC622_13340 {ECO:0000313|EMBL:KMY45091.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY45091.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMY45091.1}.
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DR EMBL; LFZV01000001; KMY45091.1; -; Genomic_DNA.
DR RefSeq; WP_049671514.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9GF49; -.
DR STRING; 1679169.AC622_13340; -.
DR PATRIC; fig|1679169.3.peg.2860; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000036953; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06573; PASTA; 1.
DR Gene3D; 1.10.150.770; -; 1.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF19; STAGE V SPORULATION PROTEIN D; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036953};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 579..637
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 639 AA; 70168 MW; 7E227BCFC31C6EBE CRC64;
MRASNHTVRK RLIAALLIGL GVFLVIDLRL GYVQIYMGNY LTDLAKDSWS RNIPFEPKRG
EIKDRNGVVY ATNKSAPTVW VVPRQVKDPA ETAKQLAAVL NMQTEKAYKL ITTNTSIVKI
PEGRKISHGK AKAVRNLDLS GVYIAEDSIR YYPKGSALAH VLGFAGIDNQ GLMGLELAYE
DELKGNKGYV KFYADAKGKR MENMADDYKS PLNGYDLTLT VDNRIQTIIE REMDIAQETY
NPDGIVGVAV NPNTGEILAM SSRPTFDPAN FRNVAPEIYN RNLPVWSTYE PGSTFKIITL
AAALEEKKVD LQNDRFYDGG YVKVGGANLR CWKRGGHGSE SFLEVVQNSC NPGFVELGER
LGKDKLFNYI HDFGFGEKTG IDLQGEGKGI LFNVDRVGPV EQATTAFGQG VSVTPIQQVM
AVSAAVNGGT LYTPYIAKEI KDPATGETIM KKSPKAKRQV ISKETSKEIR RALETVVAKG
SGKGAFVDGY RVGGKTGTAQ KAQNGRYLEN NFIVSFIGFA PADDPQIVVY IAIDNPKGTV
QFGGVVAAPI VGRIMKDSLP ALGIKPRKDQ VEKEKTYLDP VEEEVPDLVG LTLRDLSEQY
SRFKIVTSGK GSRIVQQSPK PGVKLKEGST IRIYLDEDE
//
